Structure analysis

Structure of FcgammaRI in complex with Fc reveals the importance of glycan recognition for high affinity IgG binding

X-ray diffraction
3.485Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero trimer
Accessible surface area: 39400.4 Å2
Buried surface area: 9421.07 Å2
Dissociation area: 2,229.03 Å2
Dissociation energy (ΔGdiss): -2.19 kcal/mol
Dissociation entropy (TΔSdiss): 26.73 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-134855
Assembly 2 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 38517.29 Å2
Buried surface area: 10317.13 Å2
Dissociation area: 2,193.23 Å2
Dissociation energy (ΔGdiss): -4.73 kcal/mol
Dissociation entropy (TΔSdiss): 26.69 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-134855

Macromolecules

Chains: A, B, C, D
Length: 219 amino acids
Theoretical weight: 24.7 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P01857 (Residues: 112-328; Coverage: 54%)
Gene name: IGHG1
Pfam: Immunoglobulin C1-set domain
InterPro:
CATH: Immunoglobulins

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Chains: E, F
Length: 275 amino acids
Theoretical weight: 31.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P12314 (Residues: 21-289; Coverage: 75%)
Gene names: FCG1, FCGR1, FCGR1A, IGFR1
Pfam:
InterPro:
CATH: Immunoglobulins

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